JPH11292743A - Primary lotion for permanent wave - Google Patents

Abstract

PROBLEM TO BE SOLVED: To provide a primary lotion for permanent wave protecting damage of hair in treatment, and giving excellent wave and excellent gloss and moisture to the hair after treatment. SOLUTION: This primary lotion for permanent wave inclucling a reducing agent and a hydrolyzed peptide obtained by hydrolysis of protein originating from natural product such as animal, plants or microorganism, or a cystine- introduced peptide obtained by introducing 5 to 18 mole%, of cystine based on the whole amino acids to the peptide or its derivative. The preferable amount of the cystine-introduced peptide included in the primary lotion is 0.5 to 20 wt.%.

Description

DETAILED DESCRIPTION OF THE INVENTION

[0001]

[0001] The present invention relates to a first agent for permanent waving, and more particularly to a first agent for permanent waving capable of imparting an excellent wave to hair while preventing damage to hair and scalp.

[0002]

2. Description of the Related Art Permanent waving agents generally used in the prior art include aqueous solutions mainly containing a reducing agent such as thioglycolic acid or cysteine in an aqueous solution containing a basic agent such as ammonia, monoethanolamine or triethanolamine. The first agent was prepared by adding a substance to adjust the pH to 8 to 10, and the second agent was an aqueous solution of an oxidizing agent such as sodium bromate or hydrogen peroxide.

[0003] The mechanism of waving hair with such a permanent waving agent is as follows.
Usually, the first agent is applied to the hair, the hair is wound around a rod and the hair is curled, and the first agent is used to reduce the disulfide bond of cystine contained in keratin, which is a constituent protein (protein) of the hair. A mercapto group is formed, and then the mercapto group is oxidized by a second agent to form a disulfide bond at a new position on the hair, thereby immobilizing the wave.

[0004] However, in the case of using such a permanent wave agent, the disulfide bond of cystine cleaved by the reducing agent of the first agent completely forms the disulfide bond by the subsequent oxidation of the second agent. The cystine is not always regenerated, and part of the mercapto group generated by the treatment with the first agent undergoes excessive oxidation by the second agent, and reacts with the mercapto group of thioglycolic acid or cysteine remaining in the hair. Side reactions such as the formation of disulfide bonds. As a result, damage occurs such as elution of a part of the keratin protein in the hair and physical and chemical changes in other parts of the hair. As a result, the hair not only gives an uncomfortable feeling and a crisp feeling, but also causes a great deal of damage to the hair.

[0005] The degree of such hair damage is related to the waving effect, and the first agent containing a thioglycolic acid-based reducing agent such as thioglycolic acid or thioglycolate as the main agent has a waving effect. Although the effect is excellent,
There is a problem that hair damage is very large.

[0006] Therefore, a silicone or a protein hydrolyzate (hydrolyzed peptide) is blended with a permanent waving agent to reduce the feeling of patiness of the hair after the permanent waving treatment, improve the combability, and improve the damaged hair. Attempts have been made to restore strength.

[0007] However, although silicones form a film on the hair to reduce the feeling of patiness on the surface of the hair, they do not have a fundamental repair effect on the damage of the hair due to the elution of keratin protein from the hair. In addition, there is a problem that the hair cannot be moistened, and that the hair is hardly waved by the silicone coating formed on the hair.

[0008] The protein hydrolyzate has an excellent effect of penetrating and forming a film on hair, repairing damaged hair, and giving the hair luster, moisture and good combability.
In addition, since the coating is made of a protein-derived peptide, there is no harm that waves are hardly applied.However, in the case of a protein hydrolyzate other than a protein hydrolyzate containing a large amount of a cystine having a disulfide bond or a cysteine having a mercapto group, the film is not harmful. However, there is a problem that the sorbent has a weak sorbing power to the hair, easily flows out by washing, and cannot exert its effect sufficiently.

[0009] Protein hydrolyzates, due to their protein origin, for example, hydrolyzed collagen is easy to form a film and has a large effect of increasing the strength of hair, and hydrolyzed silk forms a dense film on hair to give hair. Hydrolyzed wheat protein and hydrolyzed soy protein derived from vegetable proteins have the characteristics of having a strong moisturizing property and an excellent effect of giving a moist feeling to hair. Is a protein of a different kind from the keratin protein of the hair to be treated, in particular, does not contain cystine, which is contained in large amounts in keratin protein, or has a very low content, so that its sorption power on hair is weak, Although hair strength can be physically recovered by forming a film on damaged hair, it cannot be repaired chemically, and is combined with the first agent for permanent waving. And there is also a problem that it is not possible to fully exert their effects.

[0010] Among the protein hydrolysates, hydrolyzed keratin contains cystine, so that it has a high sorption property to hair as compared with hydrolyzed collagen and hydrolyzed silk, etc. Although the damage repair effect is excellent, there is a problem that it is slightly inferior to hydrolyzed collagen, hydrolyzed silk, hydrolyzed soy protein, etc. in terms of the ability to form a film and the effect of imparting gloss and moisture to hair, Even if this was blended with the first agent for permanent wave, a satisfactory product was not always obtained.

[0011]

SUMMARY OF THE INVENTION The present invention solves the above-mentioned problems of the first agent for permanent waving, prevents hair damage during permanent waving, and repairs damaged hair. Another object of the present invention is to provide a first permanent wave agent which imparts an excellent wave to hair and can impart good gloss and moisture to hair after permanent wave treatment.

[0012]

Means for Solving the Problems The present inventors have conducted intensive studies in order to solve the above-mentioned problems, and as a result, have obtained a hydrolysis obtained by hydrolyzing proteins derived from natural products such as animals, plants or microorganisms. A cysteine-introduced peptide having cysteine introduced into a peptide or its derivative and having an amount of cysteine of 5 to 18 mol% of all amino acids is used as a first permanent wave.
Prevents damage to the hair during permanent waving, repairs damaged hair and gives the hair an excellent wave, and gives the hair after the permanent waving a luster, moisture, etc. The inventors have found that the present invention can be performed, and have completed the present invention.

That is, a cysteine-introduced peptide which does not contain cystine or cysteine or whose cysteine is introduced into a hydrolyzed peptide having a low content of cystine or cysteine or a derivative thereof to enhance properties based on disulfide bonds, is absorbed onto the hair. And protects the hair during the permanent wave treatment, prevents damage to the hair due to the permanent wave treatment, repairs the damaged hair, and excels in the hair without impairing the waving action on the hair by a reducing agent or the like. This makes it possible to impart a wave to the hair after the permanent wave treatment, and to exert the effect of imparting, for example, luster and moisture to the hair which each hydrolyzed peptide or its derivative has on the hair.

[0014]

BEST MODE FOR CARRYING OUT THE INVENTION The cysteine-introduced peptide used in the present invention is, for example, a hydrolyzed peptide obtained by hydrolyzing a protein derived from a natural product such as an animal, a plant, or a microorganism, or a derivative thereof, with N, N'-. It is obtained by reacting dicarboxy-anhydrocystine in the presence of an alkali, and then reducing the cystine-introduced peptide obtained by decarboxylation using an acid. According to this method, the subsequent purification is easy because no protective group remains in the reaction solution of N, N'-dicarboxyanhydrocystine and the hydrolyzed peptide or its derivative based on decarboxylation.

The cysteine-introduced peptide used in the present invention is a hydrolyzed peptide obtained by hydrolyzing a protein derived from a natural product such as an animal, a plant or a microorganism, or a derivative thereof. Below, followed by decarboxylation using an acid. However, in the case of this method, it is necessary to protect the mercapto group of cysteine prior to the synthesis of N-carboxy-anhydrocysteine, and the hydrolysis peptide or its derivative and S-
It is troublesome as compared with the above-mentioned method involving reduction of the cystine-introduced peptide, such as the need to remove the protecting group after the reaction with the protected-N-carboxyanhydrocysteine.

The protein (protein) source of the hydrolyzed peptide or its derivative used in the present invention includes proteins derived from natural products, for example, collagen (including gelatin which is a denatured product thereof), keratin, silk fibroin (silk). ), Sericin, casein, conchiolin, elastin, egg-derived proteins such as egg yolk protein and egg white protein of chicken and soybeans, wheat, beer lees, corn, rice (rice bran), potato proteins, etc. Of plant origin, furthermore, yeast proteins of the genus Saccharomyces, Candida, Endomycopsis, yeast proteins isolated from so-called beer yeasts, sake yeasts, mushrooms (basidiomycetes) and chlorella Microorganisms such as isolated proteins can be used.

The hydrolyzed peptide used in the present invention can be obtained by hydrolyzing the above protein with an acid, an alkali, an enzyme or a combination thereof, wherein the amount of the acid, alkali or enzyme used, the reaction temperature, By appropriately selecting the reaction time and the like, the degree of amino acid polymerization of the obtained hydrolyzed peptide can be variously changed, but in consideration of the sorption property to the hair and the film forming property, the number average molecular weight is 100 to 2,000.
0, particularly preferably 150 to 10,000, and 200
~ 5000 is more preferable. That is, when the number average molecular weight of the hydrolyzed peptide is larger than the above range, the sorption property and permeability to the hair may be reduced, and when the number average molecular weight of the hydrolyzed peptide is smaller than the above range, the absorption to the hair may be reduced. Although excellent in adhesiveness and permeability, the film forming action on the hair may be reduced, and the protective action of the hair may be reduced.

In acid hydrolysis of a protein, for example,
Inorganic acids such as hydrochloric acid, sulfuric acid, phosphoric acid, nitric acid and hydrobromic acid, and organic acids such as acetic acid and formic acid are used.For alkaline hydrolysis of proteins, for example, sodium hydroxide,
Inorganic alkalis such as potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate and lithium carbonate are used. For the enzymatic hydrolysis of the protein, an acidic protease such as pepsin, proctase A and proctase B, and a neutral or alkaline protease such as papain, bromelain, thermolysin, trypsin, pronase and chymotrypsin are used. Bacterial neutral or alkaline proteases such as subtilisin and staphylococcal protease can also be used.

Derivatives of the hydrolyzed peptide include esters with an alcohol at the carboxyl group of the hydrolyzed peptide, for example, methyl ester, ethyl ester, propyl ester, isopropyl ester, lauryl ester, cetyl ester, 2-ethylhexyl ester. And esters with a hydrocarbon alcohol having 1 to 20 carbon atoms, such as, 2-hexyldecyl ester and stearyl ester.

In order to obtain a cysteine-introduced peptide, as described above, cysteine is added to the peptide as S-protected-N-carboxy-anhydrocysteine to obtain a cysteine-introduced peptide, and cystine is added to N, N'-dicarboxy. There is a method in which the peptide is added to the peptide as an anhydrous cystine to obtain a cystine-introduced peptide, and then a disulfide bond is cleaved by reduction to give a cysteine-introduced peptide. Since there is no trouble such as introduction of a cysteine or removal of a protective group after decarboxylation and high utility, a method of mainly reducing the latter cystine-introduced peptide will be described.

As in the latter method, to obtain a cystine-introduced peptide, cystine is first converted into N, N'-dicarboxy-anhydrocystine. A known method can be adopted.

For example, a chlorocarbonate such as benzyl chlorocarbonate, methyl chlorocarbonate or allyl chlorocarbonate is first added dropwise to an aqueous solution of cystine under alkaline conditions, and the amino acid of cystine is added as shown in the following reaction formula [I]. Protect groups.

[0023]

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(Wherein R is a benzyl group, an alkyl group or an allyl group)

Next, the reaction solution is acidified with a mineral acid such as hydrochloric acid or sulfuric acid, and then the reaction product is extracted with an organic solvent such as ethyl acetate, and the organic layer is washed with a saline solution and water. Removal by concentration under reduced pressure gives cystine in which the amino group is protected.

Next, the amino-protected cystine obtained above is dissolved in a dissolvable organic solvent such as ethyl acetate, and as shown in the following reaction formula [II], under a nitrogen gas atmosphere, When carboxyl groups are converted to carbonyl chloride by reacting with thionyl chloride (instead of thionyl chloride, phosphorus trichloride, phosphorus pentachloride, etc.) and then heat-condensed at 80 ° C. or more under reduced pressure, N, N′-diamine is obtained. A carboxy anhydrous cystine is obtained.

[0027]

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In addition, cystine is reacted directly with phosgene, phosgene dimer, phosgene trimer, etc.
N'-dicarboxy anhydrous cystine can also be synthesized.

The reaction between the hydrolyzed peptide or its derivative and N, N'-dicarboxyanhydrocystine obtained as described above proceeds as shown in the following reaction formula [III].

[0030]

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(Wherein, R ′ represents various amino acid side chains, and n represents the degree of amino acid polymerization)

First, an aqueous solution of a hydrolyzed peptide or a derivative thereof is adjusted to a pH of about 10.0 to 10.5 with an alkaline agent such as an aqueous sodium hydroxide solution, and N, dissolved in a solvent such as ethyl acetate therein. N'-dicarboxy anhydrous cystine is allowed to react by dropping under ice-cooling, and at the same time, an alkaline agent such as an aqueous solution of sodium hydroxide is dropped to pH.
Is maintained at 10.0 to 10.5.

After the completion of the dropwise addition of the anhydrous N, N'-dicarboxy cystine, the reaction is completed by continuing stirring for 2 to 5 hours under ice cooling. Next, a solvent incompatible with water, such as n-hexane, is added to the reaction solution for washing, and unreacted N, N'-dicarboxyanhydrocystine is transferred to the organic layer and removed. By adjusting the pH to 3 to 4 with hydrochloric acid or the like and performing decarboxylation, a cystine-introduced peptide can be obtained. In this cystine-introduced peptide, cystine is introduced into the hydrolyzed peptide or its derivative by an amide bond between the amino group of the hydrolyzed peptide or its derivative and the carboxyl group of cystine as shown in the formula [III].

In order to obtain a cysteine-introduced peptide from the cystine-introduced peptide obtained as described above, as shown in the reaction formula [IV], the cystine-introduced peptide is reduced and disulfide bonds are reduced and cleaved to form a mercapto group. By doing.

[0035]

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The reduction is generally performed using a reducing agent, but it is also possible to use electrolytic reduction using an electrolytic device.

Examples of the reducing agent include 2-mercaptoethanol, thioglycolic acid, thioglycerol, sodium borohydride, cysteine and the like.
Further, reduction can be performed using sodium sulfite, sodium hydrogen sulfite, or the like.In this case, cystine is converted into cysteine and S-sulfocysteine. It is half of the case of the electrolytic reduction treatment.

The cystine-introduced peptide can be reduced by putting the cystine-introduced peptide in an aqueous solution of a reducing agent adjusted to an alkaline range of pH 7 to 11 by adding an alkali agent such as sodium hydroxide or potassium hydroxide (or by adding the cystine-introduced peptide aqueous solution). The cystine-introduced peptide is adjusted by adjusting the pH to 7 to 11 and adding a reducing agent therein), preferably by stirring at a temperature of 0 to 60 ° C for 1 to 36 hours under an inert gas atmosphere such as nitrogen. A cysteine-introduced peptide can be obtained by reducing the disulfide bond therein to generate a mercapto group.

When the reduction is performed by electrolytic reduction, for example, an electrolytic reduction apparatus such as a MARK-IL two-chamber fluidized-type electrolytic apparatus manufactured by Yuasa Ionics Co., Ltd. is used.

In electrolytic reduction, the reduction occurs at the cathode,
Oxidation occurs at the anode. Therefore, in the reduction operation of the present invention, the cystine-introduced peptide is introduced into the cathode cell, the electrolyte (for example, sulfuric acid having a concentration of about 3%) is introduced into the anode cell, and the two are separated by an ion exchange membrane or the like. Reduction takes place.

The cysteine-introduced peptide thus obtained is converted into a hydrolyzed peptide or a derivative thereof by an amide bond between the amino group of the hydrolyzed peptide or a derivative thereof and the carboxyl group of cysteine as shown in Formula [IV]. Cysteine has been introduced.

The cysteine-introduced peptide can also be obtained by reacting a hydrolyzed peptide or a derivative thereof with N-carboxy-anhydrocysteine. It is necessary to protect the mercapto group (-SH group) with a benzyl ester or the like, and it is necessary to remove this protecting group after the reaction with the peptide and then remove the protecting group removed from the reaction solution by solvent extraction or the like. Since the purification is complicated, the method of obtaining the cysteine-introduced peptide through the reduction of the cystine-introduced peptide is more useful and superior.

The obtained cysteine-introduced peptide solution is adjusted to a pH suitable for the purpose of use, and is contained as it is or in powder form in the first agent for permanent wave.
Or, if necessary, after purification by ion exchange resin, dialysis membrane, electrodialysis, gel filtration, ultrafiltration, etc., the first liquid for permanent wave as a liquid or powdered
It is contained in the preparation.

In the present invention, since the cysteine-introduced peptide is characterized by forming a disulfide bond with the hair, it is necessary that the cysteine content is 5 to 18 mol% of the total amino acids contained. This is because if the amount of cysteine is less than 5 mol% of the total amino acids, the amount of cysteine, that is, the mercapto group is too small to exert a specific action as a cysteine-introduced peptide. If it exceeds 18 mol%, the water solubility will be significantly reduced and handling will be difficult.

When the cysteine-introduced peptide is contained in the first agent for permanent wave, two or more cysteine-introduced peptides having different protein sources may be used. The content of the cysteine-introduced peptide in the first agent for permanent wave (the amount of the peptide incorporated in the first agent for permanent wave) is preferably 0.5 to 20% by weight, particularly preferably 1 to 10% by weight. That is, when the content of the cysteine-introduced peptide in the first agent for permanent waving is less than the above range, the peptide moiety that protects the hair to prevent damage to the hair and imparts gloss and moisture to the hair. In addition, even if the content of the cysteine-introduced peptide in the first agent for permanent wave is larger than the above range, the effect corresponding to the increase in the content may not be obtained. In addition to no increase, the hair may become sticky due to excessive adsorption of the cysteine-introduced peptide to the hair.

The reducing agent serves as a main agent for reducing and cleaving the disulfide bond of cystine in keratin, which is a constituent protein of the hair, so as to apply a wave to the hair. For example, thioglycolic acid salts such as thioglycolic acid, ammonium thioglycolate, sodium thioglycolate, monoethanolamine thioglycolate and triethanolamine thioglycolate, esters of thioglycolic acid such as glycerin thioglycolate, and cysteine , Cysteine salts such as cysteine hydrochloride and acetylcysteine, organic mercaptan compounds such as thioglycerol, thiolactic acid, thiomalic acid, cysteamine and cysteamine salt, sodium sulfite, sodium bisulfite, potassium sulfite, ammonium sulfite Such as sulfites, such as a beam is used.

These reducing agents may be used alone or in combination of two or more. The content of the reducing agent in the first agent for permanent wave is preferably 1 to 15% by weight, particularly preferably 2 to 8% by weight. That is, if the content of the reducing agent in the first agent for permanent wave is less than the above range, there is a possibility that the hair may not be able to be sufficiently waved. If the content of is more than the above range, the disulfide bond of the hair is excessively reduced, and the protein is eluted from the hair intensely, and the hair may be greatly damaged.

The first agent for permanent wave of the present invention is prepared by making the above-mentioned reducing agent and the cysteine-introduced peptide essential components, and adding them to water or a liquid containing water as a main component. Of course, the first for the prepared or in-preparation permanent wave containing a reducing agent
The cysteine-introduced peptide may be added to the agent, and the reducing agent or the cysteine-introduced peptide may be added in any order.

The first agent for permanent wave of the present invention may contain other components as appropriate in addition to the above-mentioned essential components as long as the effects of the present invention are not impaired.

Examples of these components include licorice derivatives such as glycyrrhizic acid, disodium carbenochirosone, anti-inflammatory agents such as allantoin, guaiazulene and α-bisabolol, coconut oil fatty acid diethanolamide, sorbitan monolaurate, polyoxyethylene nonyl Penetrants such as phenyl ether and benzyl alcohol; alkyl sulfates such as triethanolamine lauryl sulfate and sodium lauryl sulfate; polyoxyethylene (2EO) lauryl ether sulfate triethanolamine (EO is ethylene oxide, and EO is The numerical values indicate the number of moles of ethylene oxide added), such as polyoxyethylene alkyl ether sulfates, sodium laurylbenzenesulfonate, and triethanolamine laurylbenzenesulfonate. Alkylbenzene sulfonates such as amines, polyoxyethylene alkyl ether acetates such as sodium polyoxyethylene (3EO) tridecyl ether acetate, coconut oil fatty acid sarcosine sodium, sodium lauroylmethyl-β-alanine, sodium lauroyl-L-glutamate, Coconut oil fatty acid-
N-acyl amino acid salts such as sodium L-glutamate, sodium coconut fatty acid methyltaurate, sodium lauroylmethyltaurine, sodium alkane sulfonate ether, sodium glycerin sulfate hardened coconut fatty acid, disodium amide amide sulfosuccinate, lauryl sulfosuccinate Disodium, polyoxyethylene alkyl (12 to 16 carbon atoms) ether phosphoric acid (2 to 12 EO), sodium polyoxyethylene cetyl ether phosphate, disodium lauryl polyoxyethylene sulfosuccinate, sodium polyoxyethylene lauryl ether phosphate, etc. Anionic surfactants such as salts of 2-alkyl-N-carboxymethyl-N
-Hydroxyethylimidazolinium betaine, undecyl-N-hydroxyethylimidazolinium betaine sodium, undecyl-N-hydroxyethyl-N-
Carboxymethyl imidazolinium betaine, stearyl dihydroxyethyl betaine, stearyl dimethylamino acetate betaine, coconut fatty acid amidopropyl betaine, coconut oil alkyl-N-carboxyethyl-N-hydroxyethylimidazolinium betaine, N
Amphoteric surfactants such as coconut oil fatty acid acyl L-arginine ethyl / DL-pyrrolidone carboxylate, polyoxyethylene alkyl (C12-14) ether (7
EO), polyoxyethylene octyl phenyl ether, polyoxyethylene oleyl ether, polyoxyethylene glyceryl oleate, polyoxyethylene stearyl ether, polyoxyethylene cetyl ether, polyoxyethylene sorbitol lanolin (40
EO), nonionic surfactants such as polyoxyethylene polyoxypropylene cetyl ether, polyoxyethylene lanolin, polyoxyethylene lanolin alcohol, stearyltrimethylammonium chloride, cetyltrimethylammonium chloride, cetostearyltrimethylammonium chloride, behenyltrimethyl bromide Ammonium, cetyltrimethylammonium iodide, oleylbenzyldimethylammonium chloride, oleylbis [polyoxyethylene (15EO)] methylammonium, dialkyldimethylammonium salt, mink oil fatty acid amide propyldimethylhydroxyethylammonium chloride, alkylpyridinium salt, -γ Cationic regions such as gluconamidopropyl dimethylhydroxyethyl ammonium Active agents, cationic cellulose,
Synthetic polymers such as cationic polymers such as cationized hydroxyethyl cellulose, poly (diallyldimethylammonium chloride), polyvinylpyrrolidone and polyethyleneimine; amphoteric polymers and anionic polymers;
Isostearic acid diethanolamide, undecylenic acid monoethanolamide, oleic acid diethanolamide, tallow fatty acid monoethanolamide, stearic acid diethanolamide, stearic acid diethylaminoethylamide, coconut oil fatty acid ethanolamide, coconut oil fatty acid diethanolamide, lauric acid isopropanolamide, Thickeners such as lauric acid ethanolamide, lauric acid diethanolamide, lanolin fatty acid diethanolamide, sodium carboxymethylcellulose, hydroxyethylcellulose, carboxyvinyl polymer, carrageenan, xanthan gum, wax, paraffin, fatty acid ester, glyceride, lecithin, squalane, avocado oil Oils and fats such as animal and vegetable oils, animal and plant extracts, polysac Or a derivative thereof, a humectant such as propylene glycol, 1,3-butylene glycol, ethylene glycol, glycerin, and polyethylene glycol; a lower alcohol such as ethanol, methanol, propyl alcohol, and isopropyl alcohol; behenyl alcohol, cetyl alcohol, and stearyl alcohol. Higher alcohols, L-aspartic acid, DL-alanine, L-arginine, glycine, L
-Amino acids such as glutamic acid, L-cysteine and L-threonine, flavors, preservatives, coloring agents, chelating agents and the like.

In the first agent for permanent wave of the present invention, the amount of cysteine as an essential component is 5 to 1 in amino acids.
A protein hydrolyzate (hydrolyzed peptide) other than 8 mol% of the cysteine-introduced peptide or a derivative thereof may be contained. Such hydrolyzed peptides include collagen, keratin, silk, sericin, casein, elastin, conchiolin, soy protein, wheat protein,
Examples thereof include those obtained by hydrolyzing complex proteins containing microorganism-derived proteins, egg proteins such as egg whites and egg yolks, sugars, phosphoric acids, fats, and the like with acids, alkalis, enzymes, or a combination thereof. Further, as the derivative of the hydrolyzed peptide, N-
-Acylated derivatives or salts thereof, quaternary ammonium derivatives, silylated derivatives, peptide esters and the like.

[0052]

EFFECTS OF THE INVENTION The first agent for permanent waving of the present invention can apply a good wave to hair while maintaining a good condition of the hair without damaging the hair. That is, the cysteine-introduced peptide contained in the first agent for permanent wave prevents hair damage due to the permanent wave treatment, repairs damaged hair, and the cysteine-introduced peptide does not hinder the permanent wave treatment. It can impart excellent wave to the hair, and can impart gloss and moisture to the hair after the permanent wave treatment.

[0053]

Next, the present invention will be described specifically with reference to examples. However, the present invention is not limited to only these examples. In the following examples and the like,
The% indicating the concentration of a solution or a dispersion is a weight% unless a unit is added. Prior to the examples, a production example of a cysteine-introduced peptide used in the examples and a production of N, N'-dicarboxy-anhydrocystine used in production of the cysteine-introduced peptide are described as reference examples. Prior to the examples, a tensile strength test for hair and a method for measuring the content of cysteic acid in the hair, which are performed in the examples, are also described.

Reference Example 1 (Production example 1 of anhydrous N, N'-dicarboxy cystine) 18 g of cystine was dissolved in 150 ml of a 1N aqueous solution of sodium hydroxide, and 38.3 g of benzyl chlorocarbonate was added with stirring under ice-cooling. Dropped over minutes. During this time, the pH of the reaction solution was maintained at 9 to 10 by adding an aqueous sodium hydroxide solution. After the end of the dropping of benzyl chlorocarbonate,
Stirring was continued at room temperature for 2 hours to complete the reaction.

After completion of the reaction, the pH of the reaction solution was adjusted to 1 with dilute hydrochloric acid, and 300 ml of ethyl acetate was added to extract a reaction product. The organic layer was washed twice with 150 ml of a 2% saline solution, further washed with 75 ml of water, and then dried over 30 ml of anhydrous sodium sulfate.
g was added and the organic layer was dried. After removing anhydrous sodium sulfate by filtration, the filtrate was concentrated under reduced pressure to dryness, and the residue was recrystallized from chloroform to obtain 30 g of N, N'-dibenzyloxycarbonylcystine.

Next, this N, N'-dibenzyloxycarbonylcystine was dissolved in 267 ml of a benzene-dioxane mixture (volume ratio = 250: 17), and the mixture was stirred under a nitrogen gas atmosphere. 2 ml of thionyl chloride was added dropwise over 1 hour. After completion of the dropwise addition, the temperature of the reaction solution was raised to 55 ° C., and stirring was continued for 3 hours to complete the reaction.

After completion of the reaction, the temperature of the reaction solution was reduced to 80 under reduced pressure.
After heating and condensing for 2 hours while maintaining the temperature at ８５85 ° C., the reaction solution was washed five times with 20 ml of n-hexane, and the aqueous layer was concentrated under reduced pressure to obtain 19.3 g of N, N′-dicarboxyanhydrocystine anhydride. I got

Reference Example 2 (Production Example 2 of anhydrous N, N'-dicarboxy cystine) 12 g of cystine was dissolved in 100 ml of a 1N aqueous solution of sodium hydroxide, and 14.1 g of methyl chlorocarbonate was added to 30 ml of the solution while stirring under ice cooling. Dropped over minutes. During this time, the pH of the reaction solution was maintained at 9 to 10 by adding an aqueous sodium hydroxide solution. After the completion of the dropwise addition of methyl chlorocarbonate, stirring was continued at room temperature for 2 hours to complete the reaction.

After completion of the reaction, the pH of the reaction solution was adjusted to 1 with dilute hydrochloric acid, and 200 ml of ethyl acetate was added to extract a reaction product. The organic layer was washed twice with 100 ml of a 2% saline solution, further washed with 100 ml of water, and then dried over anhydrous sodium sulfate.
0 g was added and the organic layer was dried. After removing anhydrous sodium sulfate by filtration, the filtrate was concentrated under reduced pressure to dryness, the residue was washed with n-hexane, and dried under reduced pressure to obtain 10 g of N,
N′-dimethoxycarbonylcystine was obtained.

Next, this N, N'-dimethoxycarbonylcystine was dissolved in 30 ml of ethyl acetate, stirred under a nitrogen gas atmosphere, and 8.07 ml of thionyl chloride was added dropwise thereto over 1 hour. After completion of the dropwise addition, the temperature of the reaction solution was raised to 55 ° C., and stirring was continued for 4 hours to complete the reaction.

After completion of the reaction, the temperature of the reaction solution was reduced to 80 under reduced pressure.
After maintaining the temperature at ８５85 ° C. and performing heat condensation for 2 hours, the reaction solution was washed 5 times with 20 ml of n-hexane, and the aqueous layer was concentrated under reduced pressure to obtain 7.9 g of N, N′-dicarboxyanhydrocystine anhydride. I got

Production Example 1 (Example of producing cysteine-introduced hydrolyzed collagen) 100 g of a 30% aqueous solution of hydrolyzed collagen having a number average molecular weight of 450 (66.7 mmol as the stoichiometric mole number obtained by measurement of amino nitrogen) ) Was adjusted to pH 10.2 with an aqueous sodium hydroxide solution, and 5.8 g (20 mmol, hydrolyzed collagen) of N, N'-dicarboxyanhydrocystine prepared in Reference Example 1 was added to this solution under ice-cooling. Was added to 80 ml of ethyl acetate, and the mixture was stirred and mixed. The mixture was stirred and reacted for 3 hours. Meanwhile, the pH of the aqueous solution was maintained at 10.0 to 10.5 by adding an aqueous sodium hydroxide solution.

After the completion of the reaction, the reaction product was washed three times with 300 ml of n-hexane to remove unreacted products, and then concentrated sulfuric acid was added to the aqueous layer to adjust the pH to 4, followed by decarbonation under reduced pressure. And
An aqueous solution of cystine-introduced hydrolyzed collagen was obtained.

Next, the pH of the aqueous solution of the cystine-introduced hydrolyzed collagen was adjusted to 9 with an aqueous sodium hydroxide solution, and 31.2 g of 2-mercaptoethanol (0.4%) was added.
Mol) was added and the mixture was stirred at 50 ° C. for 20 hours to reduce. After completion of the reduction, the solution was diluted with dilute hydrochloric acid to pH 6.5.
After adjusting the concentration, 149 g of a 30% aqueous solution of cysteine-introduced hydrolyzed collagen was obtained.

A part of the cysteine-introduced hydrolyzed collagen obtained as described above was alkylated at the SH group of the cysteine residue using monoiodoacetic acid, and then completely hydrolyzed with 6N hydrochloric acid for 20 hours to obtain an amino acid autoanalyzer. As a result of analysis of amino acids by a laser, cysteine was detected as 9.4 mol% as S-carboxymethylcysteine, and cystine was detected as 4.4 mol% as half cystine. Further, when a part of the cysteine-introduced hydrolyzed collagen obtained as described above was subjected to amino acid analysis without hydrolysis with hydrochloric acid, cysteine and cystine were not detected, and the cysteine and cystine detected above were not detected. Were all shown to be bound to hydrolyzed collagen.

Since the starting hydrolyzed collagen contains no cystine or cysteine, it is apparent that all of the cystine and cysteine were introduced into the hydrolyzed collagen by the above-described cystine introduction method or cysteine introduction method. Yes, about 68% of cystine introduced
Was reduced to cysteine to form cysteine-introduced hydrolyzed collagen.

Production Example 2 (Production Example of Cysteine-Introduced Hydrolyzed Wheat Protein) Instead of hydrolyzed collagen having a number average molecular weight of 450, 100 g of a 25% aqueous solution of a hydrolyzed wheat protein having a number average molecular weight of 700 (obtained by measuring amino nitrogen) (35.7 mmol as the stoichiometric mole number obtained) and 4.2 g of N, N'-dicarboxyanhydrocystine anhydride prepared in Reference Example 1.
(14.3 mmol, 0.8 equivalent to hydrolyzed wheat protein) dissolved in 80 ml of ethyl acetate, except that an aqueous solution of cystine-introduced hydrolyzed wheat protein was prepared in the same manner as in Production Example 1. Obtained.

Next, the pH of the aqueous solution of the cystine-introduced hydrolyzed wheat protein was adjusted to 9 with an aqueous sodium hydroxide solution, 26 g of thioglycolic acid (0.28 mol) was added, and stirring was continued at 50 ° C. for 12 hours. Reduced. After completion of the reduction, the solution was adjusted to pH 6.5 with dilute hydrochloric acid, the concentration was adjusted, and the cysteine-introduced hydrolyzed wheat protein 2 was added.
120 g of a 5% aqueous solution was obtained.

A part of the cysteine-introduced hydrolyzed wheat protein obtained as described above was alkylated at the SH group of a cysteine residue using monoiodoacetic acid, and then completely hydrolyzed with 6N hydrochloric acid for 20 hours to obtain amino acid autoantigen. Amino acid analysis with an analyzer revealed that 8.5 mol% of cysteine was detected as S-carboxymethyl cysteine and 2.6 mol% of cystine was detected as half cystine. Further, when a part of the cysteine-introduced hydrolyzed wheat protein obtained as described above was subjected to amino acid analysis without hydrolysis with hydrochloric acid, cysteine and cystine were not detected, and the cysteine and cysteine detected above were not detected. All cystine was found to be bound to the hydrolyzed wheat protein.

The raw material hydrolyzed wheat protein does not contain cysteine, and cystine is 0.4% as half cystine.
Therefore, 8.5 mol% of detected cysteine was introduced into the hydrolyzed wheat protein by the cysteine introduction method described above, and 2.2% of 2.6 mol% of half cystine was detected. It is clear that the mol% was introduced into the hydrolyzed wheat protein by the cystine introduction method described above, and about 76% of the introduced cystine and cystine contained in the raw material were reduced to cysteine,
It became cysteine-introduced hydrolyzed wheat protein.

Production Example 3 (Production Example of Hydrolyzed Cystein-Introduced Silk) A 30% aqueous solution of hydrolyzed silk having a number average molecular weight of 350 instead of hydrolyzed collagen having a number average molecular weight of 450 was used.
g (85.7 mmol as the stoichiometric mole number obtained by measurement of amino nitrogen) and 6.2 g of the N, N'-dicarboxyanhydrocystine anhydride prepared in Reference Example 1 (2
1.4 mmol, 0.5 equivalent to hydrolyzed silk)
Was dissolved in 100 ml of ethyl acetate to obtain an aqueous solution of hydrolyzed cystine-introduced silk in the same manner as in Production Example 1.

Then, 33 g of 2-mercaptoethanol (0.43%) was added to the aqueous solution of hydrolyzed cystine-introduced silk.
Mol), the pH was adjusted to 10 with an aqueous sodium hydroxide solution, and the mixture was stirred at 50 ° C. for 12 hours to reduce. After the reduction was completed, the solution was adjusted to pH 6.5 with dilute hydrochloric acid, and the concentration was adjusted to 30% of the cysteine-introduced hydrolyzed silk.
119 g of an aqueous solution was obtained.

A part of the cysteine-introduced hydrolyzed silk obtained as described above is alkylated at the SH group of the cysteine residue using monoiodoacetic acid, and then 20% with 6N hydrochloric acid.
After complete hydrolysis for an hour and amino acid analysis with an amino acid autoanalyzer, 6.8 mol% of cysteine was detected as S-carboxymethylcysteine and 2.9 mol% of cystine was detected as half cystine. Further, when a part of the cysteine-introduced hydrolyzed silk obtained as described above was subjected to amino acid analysis without hydrolysis with hydrochloric acid, cysteine and cystine were not detected, and the cysteine and cystine detected above were not detected. Was found to be all bound to hydrolyzed silk.

Since the raw material hydrolyzed silk does not contain cysteine and cystine, it is apparent that all of the cysteine and cystine have been introduced into the hydrolyzed silk by the above-described cysteine introduction method or cystine introduction method. In some cases, about 70% of the introduced cystine was reduced to cysteine, resulting in cysteine-introduced hydrolyzed silk.

Production Example 4 (Production Example of Cysteine-Introduced Hydrolyzed Yeast Protein) 100 g of a 25% aqueous solution of hydrolyzed yeast protein having a number average molecular weight of 650 (37 mmol as a stoichiometric mole obtained by measurement of amino nitrogen) ) Was adjusted to pH 10.2 with an aqueous solution of sodium hydroxide, and 3.7 g of N, N'-dicarboxyanhydrocystine anhydride (13 mmol, 0 to the hydrolyzed yeast protein) prepared in Reference Example 2 was added to the solution. (0.7 equivalents) in 80 ml of ethyl acetate was added, mixed by stirring, and reacted by continuing stirring for 3 hours. Meanwhile, the pH of the aqueous solution was maintained at 10.0 to 10.5 by adding an aqueous sodium hydroxide solution.

After the completion of the reaction, the reaction product was washed three times with 200 ml of n-hexane to remove unreacted materials, and then concentrated sulfuric acid was added to the aqueous layer to adjust the pH to 4, followed by decarbonation under reduced pressure. And
The concentration was adjusted to obtain an aqueous solution of the cystine-introduced hydrolyzed yeast protein.

Next, 20 g of 2-mercaptoethanol was added to the aqueous solution of the cystine-introduced hydrolyzed yeast protein.
(0.26 mol), and p was added with aqueous sodium hydroxide solution.
H was adjusted to 10, and stirring was continued at 50 ° C. for 8 hours to reduce. After completion of the reduction, the solution was diluted with dilute hydrochloric acid to pH 6.5.
Then, the concentration was adjusted to obtain 108 g of a 25% aqueous solution of a cysteine-introduced hydrolyzed yeast protein.

A part of the cysteine-introduced hydrolyzed yeast protein obtained as described above was subjected to alkylation of the SH group of a cysteine residue using monoiodoacetic acid, followed by complete hydrolysis with 6N hydrochloric acid for 20 hours to give amino acid autolysate. Amino acid analysis with an analyzer revealed that cysteine was detected as 8.8 mol% as S-carboxymethylcysteine, and cystine was detected as 1.9 mol% as half cystine. Further, when a portion of the cysteine-introduced hydrolyzed yeast protein obtained as described above was subjected to amino acid analysis without hydrolysis with hydrochloric acid, cysteine and cystine were not detected, and the cysteine and cysteine detected above were not detected. All cystine was found to be bound to the hydrolyzing yeast protein.

Since the starting hydrolyzed yeast protein contained 0.2 mol% of half cystine, 10.5 mol% of the total amount of 10.7 mol% of cystine and cysteine detected was as described above. It is clear that the protein was introduced into the hydrolyzed yeast protein by the cystine introduction method and the cysteine introduction method. About 83% of the introduced cystine and cystine contained in the raw material were reduced to cysteine, Introduced hydrolyzed yeast protein.

[Tensile strength test of hair] The major axis and the minor axis of the part where the tensile strength of the hair is measured (the central part of the hair of 18 cm in the example) are measured with a micrometer, and the cross-sectional area is calculated. Next, 0.5m before and after the point
At intervals of m, an adhesive tape (Scotch filament tape, manufactured by Sumitomo 3M Limited) is fixed to the hair. The part to which this tape is fixed is fixed to a clamp of a tensile tester (Rheometer manufactured by Fudo Kogyo Co., Ltd.), the strength of the hair at the time of cutting is measured, and the tension per cross-sectional area is calculated from the cross-sectional area obtained previously. The strength (kgf / mm ² ) is calculated. Measure the tensile strength of 30 hairs per sample,
An average value is determined for each sample, and the results are shown by the average value.

[Amount of cysteic acid in hair] Hair 0.01
2 g of 6N hydrochloric acid is added to the resulting mixture, and the mixture is completely hydrolyzed at 105 ° C. for 20 hours. The amount of cysteic acid (μmol / g) is determined by an automatic amino acid analyzer. The amount of cysteic acid in the hair indicates the degree of damage to the hair, and the smaller the value, the less damage to the hair.

Example 1 and Comparative Examples 1 and 2 Three kinds of first agents for permanent wave shown in Table 1 were prepared, and each of the first agents for permanent wave was prepared.
The hair bundle is subjected to a permanent wave treatment using a second agent for a permanent wave composed of an aqueous sodium bromate solution, the gloss and moisture of the treated hair are evaluated, and the tensile strength of the hair and the amount of cysteic acid in the hair are examined. Was.

In Example 1, the cysteine-introduced hydrolyzed collagen produced in Production Example 1 was used as the cysteine-introduced peptide. In Comparative Example 1, hydrolyzed collagen having a number average molecular weight of 450 was used instead of cysteine-introduced collagen. In Comparative Example 2, no cysteine-introduced peptide or hydrolyzed peptide was used.

In the examples and comparative examples, the amount of each component is not the content in the prepared first agent for permanent wave, but the amount of each component because of the preparation of the first agent for permanent wave. As will be described, the blending amounts of the components in the table are based on parts by weight, and when the blending amount is not the solid content, the solid content concentration is shown in parentheses after the component name. These are the same in the following examples.

[0085]

[Table 1]

Each of the first agents for permanent wave of Example 1 and Comparative Examples 1-2 was weighed 1 g and length 18
The hair was wrapped around a 1 cm diameter rod and subjected to a permanent wave treatment using a 6% aqueous sodium bromate solution as the second agent. 10 panelists (7 women and 3 men) for the gloss and moisture of the hair after treatment
Was evaluated. Evaluation criteria, the best two points,
Next, the result is shown as an average value of 10 persons, with the good thing being 1 point and the bad thing being 0 point. In addition, each hair bundle after the sensory evaluation was subjected to a tensile strength test, and for 40 hairs, the cross-sectional area of a portion 9 cm from the end was measured, and 5 hairs each from the larger and the smaller cross-sectional area were measured. Was excluded from the test, the tensile strength of the remaining 30 hairs was measured, and the average value was determined. Further, a part of the hair after the permanent wave treatment was hydrolyzed with hydrochloric acid, and the amount of cysteic acid was measured. Table 2 shows the results.

[0087]

[Table 2]

As is clear from the results shown in Table 2, when treated with the first agent for permanent wave of Example 1 containing cysteine-introduced hydrolyzed collagen, the first agent for permanent wave of Comparative Examples 1-2 was used. Compared to the case of treatment with hair, the evaluation value of both gloss and moisture of the hair is high, the tensile strength of the hair is large, the amount of cysteic acid in the hair is small, and the cysteine-introduced hydrolyzed collagen sorbs well to the hair It has been shown to prevent hair damage during permanent wave treatment and increase the tensile strength of hair.

Example 2 and Comparative Examples 3 and 4 Three kinds of first agents for permanent wave shown in Table 3 were prepared, and each of the first agents for permanent wave was prepared.
The hair bundle is subjected to a permanent wave treatment using a second agent for a permanent wave consisting of a 30% hydrogen peroxide solution, the gloss and moisture of the treated hair are evaluated, and the tensile strength of the hair and the amount of cysteic acid in the hair are examined. Was.

In Example 2, the cysteine-introduced hydrolyzed wheat protein produced in Production Example 2 was used as the cysteine-introduced peptide, and in Comparative Example 3, the cysteine-introduced hydrolyzed wheat protein was replaced with a hydrolyzate having a number average molecular weight of 700. Wheat protein was used, and in Comparative Example 4, no cysteine-introduced peptide or hydrolyzed peptide was used at all.

[0091]

[Table 3]

Using the first agent for permanent wave of the above Example 2 and Comparative Examples 3 and 4 and the second agent for permanent wave comprising 2% hydrogen peroxide solution, the same procedure as in Example 1 was applied with a weight of 1 g. A hair bundle having a length of 18 cm was subjected to a permanent wave treatment, and the gloss and moisture of the treated hair were evaluated by ten panelists according to the same evaluation criteria as in Example 1. Also,
The tensile strength of the hair after the permanent wave treatment and the amount of cysteic acid in the hair were measured. The measurement of the tensile strength was performed by selecting 30 hairs from each hair bundle in the same manner as in Example 1. Table 4 shows the results (average values).

[0093]

[Table 4]

As is clear from the results shown in Table 4, when treated with the first agent for permanent wave of Example 2 containing the cysteine-introduced hydrolyzed wheat protein, the first agent for permanent wave of Comparative Examples 3 and 4 was treated. The evaluation value is higher for both gloss and moisture of hair than when treated with
In addition, the tensile strength of the hair is high, the amount of cysteic acid in the hair is small, the cysteine-introduced hydrolyzed wheat protein sorbs well to the hair, prevents damage to the hair during permanent wave treatment, and increases the tensile strength of the hair It was revealed.

Example 3 and Comparative Examples 5 to 6 Three kinds of first agents for permanent wave shown in Table 5 were prepared, and each of the first agents for permanent wave was prepared.
The hair bundle is subjected to a permanent wave treatment using a second agent for a permanent wave composed of an aqueous sodium bromate solution, the gloss and moisture of the treated hair are evaluated, and the tensile strength of the hair and the amount of cysteic acid in the hair are examined. Was.

In Example 3, the cysteine-introduced hydrolyzed silk prepared in Production Example 3 was used as the cysteine-introduced peptide. In Comparative Example 5, hydrolyzed silk having a number average molecular weight of 350 was used instead of the cysteine-introduced hydrolyzed silk. In Comparative Example 6, no cysteine-introduced peptide or hydrolyzed peptide was used.

[0097]

[Table 5]

Using the first agent for permanent wave of the above Example 3 and Comparative Examples 5 to 6 and the second agent for permanent wave comprising a 6% aqueous solution of sodium bromate, a weight of 1 g was used in the same manner as in Example 1. A hair bundle having a length of 18 cm was subjected to a permanent wave treatment, and the gloss and moisture of the treated hair were evaluated by ten panelists according to the same evaluation criteria as in Example 1. Further, the tensile strength of the hair after the permanent wave treatment and the amount of cysteic acid in the hair were measured. In addition,
The measurement of the tensile strength was performed by selecting 30 hairs from each hair bundle in the same manner as in Example 1. Table 6 shows the results (average values).

[0099]

[Table 6]

As is clear from the results shown in Table 6, when treated with the first agent for permanent wave of Example 3 containing cysteine-introduced hydrolyzed silk, Comparative Examples 5 to
As compared with the case of treating with the first agent for permanent wave of No. 6, the evaluation value of both gloss and moisture of the hair was higher. In the case of cysteine perm, compared to the permanent wave treatment using thioglycolic acid as a reducing agent, the damage to the hair is less, and therefore the difference in tensile strength and the amount of cysteic acid in the hair is not so large between the example and the comparative example. Although not increased, the hair treated with the first agent for permanent wave of Example 3 still has a higher tensile strength than the hair treated with the first agent for permanent wave of Comparative Examples 5 to 6, and the hair in the hair It has been shown that cystine-introduced hydrolyzed silk has a low cysteinic acid content and sorbs well to the hair, preventing damage to the hair during permanent wave treatment.

Example 4 A first agent for permanent wave having the following composition was prepared using the cysteine-introduced hydrolyzed yeast protein produced in Production Example 4 as the cysteine-introduced peptide. All amounts are based on parts by weight.

Cysteine-introduced hydrolyzed yeast protein (25%) 6.0 Sodium bisulfite 3.5 Ammonium bicarbonate 2.0 Disodium edetate 0.1 Monoethanolamine Make pH 7.2 Fragrance Appropriate amount Sterilized ion-exchanged water Total 100

Using the first agent for permanent waving of Example 4 prepared as described above, using a 6% aqueous sodium bromate solution for the second agent, and subjecting the hair to a permanent waving treatment, A good wave was imparted, and the treated hair had good luster and moisture.

 ────────────────────────────────────────────────── ─── Continuing on the front page (72) Inventor Aie Matsukawa 1-2-14 Fukuichicho, Higashiosaka-shi, Osaka Seiwa Chemical Co., Ltd.

Claims (2)

[Claims] Claims: 1. A first agent for permanent wave containing a reducing agent, wherein cysteine is introduced into a hydrolyzed peptide or a derivative thereof obtained by hydrolyzing a protein derived from a natural product such as an animal, a plant or a microorganism. A first agent for permanent wave, comprising a cysteine-introduced peptide in an amount of 5 to 18 mol% of the total amino acids. 2. The method according to claim 1, wherein the content of the cysteine-introduced peptide is 0.
The first agent for permanent wave according to claim 1, which is 5 to 20% by weight.